Research Summary: Neuropharmacology Synapses and Receptor Mechanisms

Dr. Taylor’s studies have employed spectroscopic physical methods, X ray crystallography, sequence and three dimensional structural determinations to investigate the principles of molecular recognition. He has worked with nicotinic acetylcholine receptors and acetylcholinesterase since the mid-1970’s with current interests directed to structure and dynamics as they relate to ligand design. For acetylcholinesterase (AChE), reactivating antidotes to organophosphate nerve agent and insecticide exposure are designed to confer oral bioavailability and CNS reactivation capabilities. These studies evolved from collaboration with Barry Sharpless of TSRI using AChE as the first target template for freeze-frame, click chemistry to synthesize in situ selective cholinesterase inhibitors and reactivator antidotes. Collaborative studies with nicotinic receptors also employ click-chemistry in structure- guided drug design. In this case, a soluble surrogate for the extracellular domain of the nicotinic receptor is used as the template for the in situ synthesis of novel nicotinic receptor ligands directed to the α7 subtype. More recently, Taylor has conducted studies into the structure and function of a post-synaptic adhesion protein homologous to AChE, neuroligin, and its pre- synaptic partner, neurexin. Studies employ both crystallographic and solution-based techniques and are directed to macromolecular recognition of ectodomain adhesion molecules.

Academic Achievements

Education:

B.S and Ph.D. in Physical Pharmacy University of Wisconsin; Post-doctoral fellowships NIH and Cambridge University, United Kingdom.